Anosmin 1 interacts with the prokineticin receptor 2 in vitro indicating a molecular link between both proteins in the pathogenesis of kallmann syndrome

Sexual maturation and olfactory bulb defects found in prokineticin 2 (pk2) and prokineticin receptor 2 (pkr2) mutant mice resembling the phenotypic characteristics of kallmann syndrome (ks),gave rise to the question of whether these genes would have a role in ks pathogenesis. later,mutations in both genes were identified in patients suffering from ks. the gene responsible for the x-linked form of ks,anos1,encodes the ecm protein anosmin 1. among other functions,anosmin 1 can regulate the activity of fgfr1,encoded by one of the genes involved in the autosomal transmission of ks. therefore,it has been proposed that anosmin 1 could interact with pkr2 to modulate its activity. we present the first evidence supporting this hypothesis and report the interaction of full-length anosmin 1 with three extracellular domains of pkr2. a truncated anosmin 1 protein comprising the first three domains of the protein interacts with the second extracellular loop of pkr2,involved in pk2 binding. finally,last three fniii repeats of anosmin 1 also interacted with the pkr2 domains that interacted with full-length anosmin 1. our data represent a molecular link between two of the genes involved in ks pathogenesis. © 2016 bentham science publishers.